ID I0A203_FERFK Unreviewed; 203 AA.
AC I0A203;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Indolepyruvate:ferredoxin oxidoreductase subunit beta {ECO:0000313|EMBL:AFH43010.1};
GN OrderedLocusNames=FFONT_1022 {ECO:0000313|EMBL:AFH43010.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43010.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH43010.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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DR EMBL; CP003423; AFH43010.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A203; -.
DR STRING; 1163730.FFONT_1022; -.
DR KEGG; ffo:FFONT_1022; -.
DR eggNOG; arCOG01602; Archaea.
DR HOGENOM; CLU_087284_1_1_2; -.
DR InParanoid; I0A203; -.
DR OrthoDB; 53326at2157; -.
DR Proteomes; UP000007391; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR PANTHER; PTHR43854; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR PANTHER; PTHR43854:SF1; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AFH43010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007391};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..193
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
SQ SEQUENCE 203 AA; 22446 MW; 9187043982CFF5DA CRC64;
MKEYNIIISG VGGQGVITIA NLIGLAAFKQ GIKARVGEIH GLSQRFGSVF THVRIGEDVY
SSIVPLGRGD LLISLEAIET LRYLKYMKKD GLILMNTLMT EPFKTISVDP KIADINEIKK
MMKSAFDGKI LIINGNELTE KLKNSLLLNT AIIGIALTIP GFPLKEESIK ASIEEMFDRK
YVELNIRALE VGMNYGKEIL STQ
//
